Chemical structure of peptidoglycan in Selenomonas ruminantium: cadaverine links covalently to the D-glutamic acid residue of peptidoglycan.
The peptidoglycan of Selenomonas ruminantium, a strictly anaerobic bacterium, contains cadaverine (Y. Kamio, Y. Itoh, Y. Terawaki, and T. Kusano, J. Bacteriol. 145:122-128, 1981). This report describes the chemical structure of the peptidoglycan of this bacterium. The [14C]cadaverine-labeled peptidoglycan was degraded with the lytic enzymes prepared from Streptomyces albus G into three small fragments including a major fragment (band A compound). Bank A compound was composed of L-alanine, D-glutamic acid, meso-diaminopimelic acid, D-alanine, and cadaverine in the molar ratio 0.98:1.0:1.0:0.98:0.97. Diaminopimelic acid, L-alanine, and cadaverine were N-terminal residues in band A compound. When the [14C]cadaverine-labeled band A compound was subjected to partial acid hydrolysis, two peptide fragments were obtained. One of them consisted of diaminopimelic acid and D-alanine; diaminopimelic acid was the N-terminal amino acid, and the other fragment was composed of L-alanine, D-glutamic acid, and cadaverine, of which L-alanine and cadaverine were N-terminal. These results lead us to conclude that the primary peptide structure of band A compound is L-alanyl-D-glutamyl-meso-diaminopimelyl-D-alanine and that cadaverine links covalently to the D-glutamic acid residue.
D000595:Amino Acid Sequence; D001322:Autoanalysis; D002103:Cadaverine / Q000032:analysis; D002850:Chromatography, Gel; D002854:Chromatography, Paper; D004586:Electrophoresis; D005971:Glutamates / Q000032:analysis; D006089:Gram-Negative Anaerobic Bacteria / Q000648:ultrastructure*; D006867:Hydrolases / Q000378:metabolism; D006868:Hydrolysis; D010457:Peptidoglycan; D011868:Radioisotopes; D013305:Streptomyces griseus / Q000201:enzymology
D005971:Glutamates; D010457:Peptidoglycan; D011868:Radioisotopes; D006867:Hydrolases; D002103:Cadaverine